Header list of 2bun.pdb file
Complete list - y 2 2 Bytes
HEADER APPA 15-JUN-05 2BUN
TITLE SOLUTION STRUCTURE OF THE BLUF DOMAIN OF APPA 5-125
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APPA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BLUF DOMAIN, RESIDUES 5-125;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES 2.4.1;
SOURCE 3 ORGANISM_TAXID: 272943;
SOURCE 4 VARIANT: RK1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PLICHIS
KEYWDS APPA, FAD, ALPHA-BETA SANDWICH, BLUF DOMAIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.S.GRINSTEAD,S.-T.HSU,W.LAAN,A.M.J.J.BONVIN,K.J.HELLINGWERF,
AUTHOR 2 R.BOELENS,R.KAPTEIN
REVDAT 4 02-MAY-18 2BUN 1 SOURCE JRNL REMARK
REVDAT 3 24-FEB-09 2BUN 1 VERSN
REVDAT 2 20-DEC-06 2BUN 1 JRNL
REVDAT 1 07-DEC-05 2BUN 0
JRNL AUTH J.S.GRINSTEAD,S.T.HSU,W.LAAN,A.M.BONVIN,K.J.HELLINGWERF,
JRNL AUTH 2 R.BOELENS,R.KAPTEIN
JRNL TITL THE SOLUTION STRUCTURE OF THE APPA BLUF DOMAIN: INSIGHT INTO
JRNL TITL 2 THE MECHANISM OF LIGHT-INDUCED SIGNALING.
JRNL REF CHEMBIOCHEM V. 7 187 2006
JRNL REFN ISSN 1439-4227
JRNL PMID 16323221
JRNL DOI 10.1002/CBIC.200500270
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-
REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 2BUN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1290024518.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310.0; 310.0; 310.0; 310.0
REMARK 210 PH : 7.4; 7.4; 7.4; 7.4
REMARK 210 IONIC STRENGTH : NULL; NULL; NULL; NULL
REMARK 210 PRESSURE : 1.0 ATM; 1.0 ATM; 1.0 ATM; 1.0
REMARK 210 ATM
REMARK 210 SAMPLE CONTENTS : 5% D2O/95% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TRIPLE RESONANCE; HCCH
REMARK 210 -COSY; HCCH-TOCSY; HYDROGEN-
REMARK 210 DEUTERIUM EXCHANGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 700 MHZ; 600 MHZ; 750
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY, ARIA, CNS
REMARK 210 METHOD USED : ARIA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED APPA 5-125
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 THR A 10 -159.18 62.31
REMARK 500 1 ALA A 25 104.41 23.87
REMARK 500 1 ASP A 82 -147.16 -64.66
REMARK 500 1 ARG A 83 -19.21 154.23
REMARK 500 1 SER A 86 -56.57 -5.59
REMARK 500 1 VAL A 88 70.40 35.19
REMARK 500 1 ILE A 90 -72.42 -48.24
REMARK 500 1 LEU A 91 -14.40 58.69
REMARK 500 1 LYS A 98 174.36 55.97
REMARK 500 1 ARG A 99 -31.08 152.45
REMARK 500 1 SER A 109 -159.41 -131.57
REMARK 500 1 CYS A 110 89.61 -67.42
REMARK 500 1 SER A 111 169.47 71.39
REMARK 500 1 ALA A 113 116.44 73.89
REMARK 500 1 ASP A 114 -38.93 75.64
REMARK 500 1 ALA A 121 77.88 -102.17
REMARK 500 2 THR A 10 -170.88 70.65
REMARK 500 2 ASP A 15 53.12 -112.84
REMARK 500 2 LEU A 24 53.93 -108.06
REMARK 500 2 ALA A 25 110.61 -1.69
REMARK 500 2 GLN A 58 -2.46 67.82
REMARK 500 2 ARG A 83 -33.95 -165.85
REMARK 500 2 ASN A 87 -35.50 -134.50
REMARK 500 2 VAL A 88 83.61 41.56
REMARK 500 2 LEU A 91 -26.24 68.46
REMARK 500 2 LYS A 98 -164.68 55.21
REMARK 500 2 ALA A 102 -16.22 61.56
REMARK 500 2 LEU A 108 -79.64 -79.52
REMARK 500 2 SER A 109 -40.92 68.77
REMARK 500 2 CYS A 110 -29.45 -166.31
REMARK 500 2 GLU A 112 -72.86 66.72
REMARK 500 2 ASP A 114 -70.16 -104.82
REMARK 500 2 ARG A 116 -4.12 69.80
REMARK 500 2 SER A 123 104.59 68.83
REMARK 500 3 THR A 10 -162.80 57.48
REMARK 500 3 THR A 12 -15.99 69.35
REMARK 500 3 SER A 14 -77.85 -177.89
REMARK 500 3 LEU A 24 69.84 -112.85
REMARK 500 3 ALA A 25 124.93 -23.99
REMARK 500 3 GLN A 49 40.39 72.00
REMARK 500 3 GLN A 58 76.03 62.57
REMARK 500 3 ASP A 82 -148.74 -86.50
REMARK 500 3 ARG A 83 -32.58 175.75
REMARK 500 3 SER A 86 -13.83 -44.06
REMARK 500 3 ASN A 87 -51.87 -144.36
REMARK 500 3 ILE A 90 -73.45 -51.09
REMARK 500 3 LEU A 91 -13.62 62.84
REMARK 500 3 LYS A 98 -170.66 58.11
REMARK 500 3 ARG A 99 48.01 82.23
REMARK 500 3 ARG A 100 -66.37 -101.51
REMARK 500
REMARK 500 THIS ENTRY HAS 370 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 100 0.09 SIDE CHAIN
REMARK 500 2 ARG A 32 0.08 SIDE CHAIN
REMARK 500 3 ARG A 84 0.08 SIDE CHAIN
REMARK 500 4 ARG A 22 0.07 SIDE CHAIN
REMARK 500 7 ARG A 84 0.12 SIDE CHAIN
REMARK 500 10 ARG A 124 0.08 SIDE CHAIN
REMARK 500 12 ARG A 47 0.08 SIDE CHAIN
REMARK 500 12 ARG A 84 0.08 SIDE CHAIN
REMARK 500 17 ARG A 84 0.08 SIDE CHAIN
REMARK 500 17 ARG A 100 0.12 SIDE CHAIN
REMARK 500 18 ARG A 83 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A1126
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6692 RELATED DB: BMRB
DBREF 2BUN A 5 125 UNP Q53119 Q53119_RHOSH 5 125
SEQADV 2BUN HIS A 68 UNP Q53119 ARG 68 CONFLICT
SEQADV 2BUN SER A 77 UNP Q53119 THR 77 CONFLICT
SEQADV 2BUN SER A 95 UNP Q53119 PRO 95 CONFLICT
SEQRES 1 A 121 LEU GLU ALA ASP VAL THR MET THR GLY SER ASP LEU VAL
SEQRES 2 A 121 SER CYS CYS TYR ARG SER LEU ALA ALA PRO ASP LEU THR
SEQRES 3 A 121 LEU ARG ASP LEU LEU ASP ILE VAL GLU THR SER GLN ALA
SEQRES 4 A 121 HIS ASN ALA ARG ALA GLN LEU THR GLY ALA LEU PHE TYR
SEQRES 5 A 121 SER GLN GLY VAL PHE PHE GLN TRP LEU GLU GLY HIS PRO
SEQRES 6 A 121 ALA ALA VAL ALA GLU VAL MET SER HIS ILE GLN ARG ASP
SEQRES 7 A 121 ARG ARG HIS SER ASN VAL GLU ILE LEU ALA GLU GLU SER
SEQRES 8 A 121 ILE ALA LYS ARG ARG PHE ALA GLY TRP HIS MET GLN LEU
SEQRES 9 A 121 SER CYS SER GLU ALA ASP MET ARG SER LEU GLY LEU ALA
SEQRES 10 A 121 GLU SER ARG GLN
HET FAD A1126 84
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 2 FAD C27 H33 N9 O15 P2
HELIX 1 1 THR A 30 GLN A 49 1 20
HELIX 2 2 HIS A 68 GLN A 80 1 13
HELIX 3 3 ASP A 114 GLY A 119 5 6
SHEET 1 AA 4 THR A 51 SER A 57 0
SHEET 2 AA 4 VAL A 60 GLY A 67 -1 O VAL A 60 N SER A 57
SHEET 3 AA 4 LEU A 16 SER A 23 -1 O VAL A 17 N GLY A 67
SHEET 4 AA 4 GLU A 89 ILE A 96 -1 O GLU A 89 N ARG A 22
SITE 1 AC1 14 TYR A 21 ILE A 37 THR A 40 SER A 41
SITE 2 AC1 14 HIS A 44 ASN A 45 PHE A 61 GLN A 63
SITE 3 AC1 14 VAL A 75 HIS A 78 ILE A 79 ARG A 84
SITE 4 AC1 14 HIS A 85 TRP A 104
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - y 2 2 Bytes